Dissecting conformational contributions to glycosidase catalysis and inhibition

scientific article published on 10 July 2014

Dissecting conformational contributions to glycosidase catalysis and inhibition is …
instance of (P31):
scholarly articleQ13442814
review articleQ7318358

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P356DOI10.1016/J.SBI.2014.06.003
P932PMC publication ID4220041
P698PubMed publication ID25016573
P5875ResearchGate publication ID263860289

P50authorGideon DaviesQ18342394
Spencer WilliamsQ42690198
Andrew James ThompsonQ43144579
Gaetano SpecialeQ55978955
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Aldehydes as Inhibitors of PapainQ54636763
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Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentiiQ71541016
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Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanaseQ27618772
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Distortion of a cellobio-derived isofagomine highlights the potential conformational itinerary of inverting beta-glucosidasesQ27641245
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Mechanistic insights into a Ca2+-dependent family of α-mannosidases in a human gut symbiontQ27659017
Analysis of a New Family of Widely Distributed Metal-independent α-Mannosidases Provides Unique Insight into the Processing of N -Linked GlycansQ27667236
Structural and mechanistic insight into N-glycan processing by endo-α-mannosidaseQ27676550
Analysis of Keystone Enzyme in Agar Hydrolysis Provides Insight into the Degradation (of a Polysaccharide from) Red SeaweedsQ27677860
Human α-l-iduronidase uses its own N -glycan as a substrate-binding and catalytic moduleQ27679724
Structural snapshots illustrate the catalytic cycle of β-galactocerebrosidase, the defective enzyme in Krabbe diseaseQ27680741
Combined Inhibitor Free-Energy Landscape and Structural Analysis Reports on the Mannosidase Conformational CoordinateQ27680888
The reaction coordinate of a bacterial GH47 α-mannosidase: a combined quantum mechanical and structural approachQ27682479
Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortionQ27683501
Influenza neuraminidase operates via a nucleophilic mechanism and can be targeted by covalent inhibitorsQ27684045
Mechanism-based covalent neuraminidase inhibitors with broad-spectrum influenza antiviral activityQ27684054
X-ray crystallographic studies of family 11 xylanase Michaelis and product complexes: implications for the catalytic mechanismQ27688881
Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs diseaseQ27732881
The conformational free energy landscape of beta-D-glucopyranose. Implications for substrate preactivation in beta-glucoside hydrolasesQ28240539
Mycobacterium tuberculosis strains possess functional cellulasesQ28487153
Rational design of potent sialidase-based inhibitors of influenza virus replicationQ29616647
The carbohydrate-active enzymes database (CAZy) in 2013Q29617118
The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design.Q30356303
Turnover is rate-limited by deglycosylation for Micromonospora viridifaciens sialidase-catalyzed hydrolyses: conformational implications for the Michaelis complexQ34164726
Conformational analyses of the reaction coordinate of glycosidasesQ34216875
Emerging principles for the therapeutic exploitation of glycosylation.Q34395447
Thiooligosaccharides as tools for structural biologyQ34518281
How sugars pucker: electronic structure calculations map the kinetic landscape of five biologically paramount monosaccharides and their implications for enzymatic catalysis.Q35075956
Covalent inhibitors of glycosidases and their applications in biochemistry and biologyQ37171562
P921main subjectenzymeQ8047
biomedical investigative techniqueQ66648976
P304page(s)1-13
P577publication date2014-07-10
2014-10-01
P1433published inCurrent Opinion in Structural BiologyQ15758416
P1476titleDissecting conformational contributions to glycosidase catalysis and inhibition
P478volume28

Reverse relations

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